Structural analysis of botulinum neurotoxin type E catalytic domain and its mutant Glu212→Gln reveals the pivotal role of the Glu212 carboxylate in the catalytic pathway

Biochemistry

Volumn 43, Issue 21, 2004, Pages 6637-6644

  Agarwal, Rakhi ^a   Eswaramoorthy, Subramaniam ^a   Kumaran, Desigan ^a   Binz, Thomas ^b   Swaminathan, Subramanyam ^a  

^a BROOKHAVEN NATIONAL LABORATORY   (United States)

^b HANNOVER MEDICAL SCHOOL   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYST ACTIVITY; CHEMICAL BONDS; DRUG PRODUCTS; ENZYME INHIBITION; ENZYME KINETICS; NEUROLOGY; STRUCTURE (COMPOSITION);

BOTULINUM NEUROTOXIN TYPE E; NUCLEOPHILICITY;

BIOCHEMISTRY;

BOTULINUM TOXIN; BOTULINUM TOXIN A; BOTULINUM TOXIN B; BOTULINUM TOXIN C; BOTULINUM TOXIN D; BOTULINUM TOXIN E; BOTULINUM TOXIN F; BOTULINUM TOXIN G; CARBOXYLIC ACID; GLUTAMIC ACID; GLUTAMINE; UNCLASSIFIED DRUG; VACCINE;

ARTICLE; CATALYSIS; CHEMICAL BOND; CLOSTRIDIUM BOTULINUM; CRYSTAL STRUCTURE; DELETION MUTANT; DNA MODIFICATION; GENETIC CONSERVATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; SEQUENCE HOMOLOGY; SEROTYPE; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; BOTULINUM TOXINS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; GLUTAMIC ACID; GLUTAMINE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; POINT MUTATION; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY, AMINO ACID;

BACTERIA (MICROORGANISMS); CLOSTRIDIUM; CLOSTRIDIUM BOTULINUM; POSIBACTERIA;

EID: 2542517864     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi036278w     Document Type: Article

References (28)

1. Schiavo, G., Matteoli, M., and Montecucco, C. (2000) Neurotoxins affecting neuroexocytosis, Physiol. Rev. 80, 717-766.
2. Schiavo, G., Santucci, A., Dasgupta, B. R., Metha, P. P., Jontes, J., Benfenati, F., Wilson, M. C., and Montecucco, C. (1993) Botulinum neurotoxins serotypes A and E cleave SNAP-25 at distinct COOH-terminal peptide bonds, FEBS Lett. 335, 99-103.
3. Binz, T., Blasi, J., Yamasaki, S., Baumeister, A., Link, E., Sudhof, T. C., Jahn, R., and Niemann, H. (1994) Proteolysis of SNAP-25 by Types E and A botulinum neurotoxins, J. Biol. Chem. 269, 1617-1620.
4. Vaidyanathan, V. V., Yoshino, K., Jahnz, M., Dorries, C., Bade, S., Nauenburg, S., Niemann, H., and Binz, T. (1999) Proteolysis of SNAP-25 isoforms by botulinum neurotoxin types A, C, and E: Domains and amino acid residues controlling the formation of enzyme-substrate complexes and cleavage, J. Neurochem. 72, 327-337.
5. Montecucco, C., and Schiavo, G. (1995) Structure and function of tetanus and botulinum neurotoxins, Q. Rev. Biophys. 28, 423-472.
6. Lacy, D. B., Tepp, W., Cohen, A. C., DasGupta, B. R., and Stevens, R. C. (1998) Crystal structure of botulinum neurotoxin type A and implications for toxicity, Nat. Struct. Biol. 5, 898-902.
7. Swaminathan, S., and Eswaramoorthy, S. (2000) Structural analysis of the catalytic and binding sites of Clostridium botulinum neurotoxin B, Nat. Struct. Biol. 7, 693-699.
8. Hanson, M. A., and Stevens, R. C. (2000) Cocrystal structure of synaptobrevin-II bound to botulinum neurotoxin type B at 2.0 A resolution, Nat. Struct. Biol. 7, 687-692.
9. c of tetanus neurotoxin, Nat. Struct. Biol. 4, 788-792.
10. Emsley, P., Fotinou, C., Black, I., Fairweather, N. F., Charles, I. G., Watts, C., Hewitt, E., and Isaacs, N. W. (2000) The structures of the H(C) fragment of tetanus toxin with carbohydrate subunit complexes provide insight into ganglioside binding, J. Biol. Chem. 275, 8889-8894.
11. Agarwal, R., Eswaramoorthy, S., Kumaran, D., Dunn, J. J., and Swaminathan, S. (2004) Cloning, high level expression, purification and crystallization of the full length Clostridium botulinum neurotoxin type E light chain, Protein Expr. Purif. 34, 95-102.
12. Vagin, A., and Teplyakov, A. (2000) An approach to multi-copy search in molecular replacement, Acta Crystallogr. D56, 1622-1624.
13. Otwinowski, Z., and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode, Methods Enzymol. 276, 307-326.
14. Furey, W., and Swaminathan, S. (1997) PHASES-95: A program package for the processing and analysis of diffraction data from macromolecules., Methods Enzymol. 276, 590-620.
15. De La Fortelle, E., and Bricogne, G. (1997) Maximum-likelihood heavy atom parameter refinement in the MIR and MAD methods, Methods Enzymol. 276, 472-493.
16. Cowtan, K. (1994) Joint CCP4 ESF-EACBM Newsl. Protein Crystallogr. 31, 34-38.
17. Perrakis, A., Morris, R., and Lamzin, V. S. (1999) Automated protein model building combined with iterative structure refinement, Nat. Struct. Biol. 6, 458-463.
18. Brunger, A. T., Adams, P. D., Clore, G. M., Delano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J. S., Kuszwewski, J., Nilges, M., Pannu, N. S., Read, R. J., Rice, L. M., Somonsom, T., and Warren, G. L. (1998) Crystallography & NMR system: a new software suite for macromolecular structure determination, Acta Crystallogr. D54, 905-921.
19. Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) PROCHECK: a program to check the stereochemical quality for assessing the accuracy of protein structures, J. Appl. Crystallogr. 26, 283-291.
20. Washbourne, P., Pellizzari, R., Baldini, G., Wilson, M. C., and Montecucco, C. (1997) Botulinum neurotoxin A and E require the SNARE motif in SNAP-25 for proteolysis, FEBS Lett. 418, 1-5.
21. Rigoni, M., Caccin, P., Johnson, E. A., Montecucco, C., and Rossetto, O. (2001) Site-directed mutagenesis identifies active-site residues of the light chain of botulinum neurotoxin type A, Biochem. Biophys. Res. Commun. 288, 1231-1237.
22. Ahmed, S. A., and Smith, L. A. (2000) Light chain of botulinum A neurotoxin expressed as an inclusion body from a synthetic gene is catalytically and functionally active, J. Protein Chem. 19, 475-487.
23. DasGupta, B. R., and Foley, J. (1989) C. Botulinum neurotoxin types A and E: isolated light chain breaks down into two fragments. Comparison of their amino acid sequences with tetanus neurotoxin, Biochemie 71, 1193-1200.
24. 365 of the botulinum neurotoxin type A light chain are involved in transition state stabilization, Biochemistry 41, 1717-1723.
25. Li, L., Binz, T., Niemann, H., and Singh, B. R. (2000) Probing the mechanistic role of glutamate residues in the zinc-binding motif of type A botulinum neurotoxin light chain, Biochemistry 39, 2399-2405.
26. 2 anion, J. Chem. Phys. 116, 9672-9676.
27. Swaminathan, S., Eswaramoorthy, S., and Kumaran, D. (2004) Structure and enzymatic activity of botulinum neurotoxins, Mov. Disord. 19 (Suppl. 8), S17-S22.
28. Rossetto, O., Caccin, P., Rigoni, M., Tonello, F., Bortoletto, N., Stevens, R. C., and Montecucco, C. (2001) Active-site mutagenesis of tetanus neurotoxin implicates TYR-375 and GLU-271 in metalloproteolytic activity, Toxicon 39, 1151-1159.